3wl7: Difference between revisions
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''' | ==The complex structure of pOPH S172C with ligand, ACA== | ||
<StructureSection load='3wl7' size='340' side='right' caption='[[3wl7]], [[Resolution|resolution]] 1.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wl7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WL7 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=P2D:PENTANE-2,4-DIONE'>P2D</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wl5|3wl5]], [[3wl6|3wl6]], [[3wl8|3wl8]], [[3wla|3wla]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-diketone_hydrolase Beta-diketone hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.7 3.7.1.7] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wl7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wl7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wl7 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ever-increasing production and use of polyvinyl alcohol (PVA) threaten our environment. Yet PVA can be assimilated by microbes in two steps: oxidation and cleavage. Here we report novel alpha/beta-hydrolase structures of oxidized PVA hydrolase (OPH) from two known PVA-degrading organisms, Sphingopyxis sp. 113P3 and Pseudomonas sp. VM15C, including complexes with substrate analogues, acetylacetone and caprylate. The active site is covered by a lid-like beta-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of beta-diketone, although it has a catalytic triad similar to that of most alpha/beta-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving beta-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications. | |||
Structural insights into enzymatic degradation of oxidized polyvinyl alcohol.,Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G Chembiochem. 2014 Sep 5;15(13):1882-6. doi: 10.1002/cbic.201402166. Epub 2014 Jul, 8. PMID:25044912<ref>PMID:25044912</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Beta-diketone hydrolase]] | |||
[[Category: Chan, H C.]] | |||
[[Category: Chen, J.]] | |||
[[Category: Du, G C.]] | |||
[[Category: Guo, R T.]] | |||
[[Category: Huang, C H.]] | |||
[[Category: Jia, D X.]] | |||
[[Category: Ko, T P.]] | |||
[[Category: Li, J H.]] | |||
[[Category: Liu, L.]] | |||
[[Category: Ren, F F.]] | |||
[[Category: Wang, A H.J.]] | |||
[[Category: Yang, Y.]] | |||
[[Category: Alpha/beta-hydrolase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Oxi-polyvinyl alcohol hydrolase]] | |||
Revision as of 13:22, 24 September 2014
The complex structure of pOPH S172C with ligand, ACAThe complex structure of pOPH S172C with ligand, ACA
Structural highlights
Publication Abstract from PubMedThe ever-increasing production and use of polyvinyl alcohol (PVA) threaten our environment. Yet PVA can be assimilated by microbes in two steps: oxidation and cleavage. Here we report novel alpha/beta-hydrolase structures of oxidized PVA hydrolase (OPH) from two known PVA-degrading organisms, Sphingopyxis sp. 113P3 and Pseudomonas sp. VM15C, including complexes with substrate analogues, acetylacetone and caprylate. The active site is covered by a lid-like beta-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of beta-diketone, although it has a catalytic triad similar to that of most alpha/beta-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving beta-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications. Structural insights into enzymatic degradation of oxidized polyvinyl alcohol.,Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G Chembiochem. 2014 Sep 5;15(13):1882-6. doi: 10.1002/cbic.201402166. Epub 2014 Jul, 8. PMID:25044912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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